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                    <h3 id="dir0p" style="color:#fffea4;padding-left: 10%;font-size:1.8rem;">
                        Engineering</h3>
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                                Overview
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                                Engineering Success</p>
                            <p id="dir2p1j" class="mlyj" style="color:#ffffff;">BBa_K3740050</p>
                            <p id="dir2p1j1" class="mlej" style="color:#ffffff;">Design </p>
                            <p id="dir2p1j2"class="mlej" style="color:#ffffff;"> Strategy</p>
                            <p id="dir2p1j3"class="mlej" style="color:#ffffff;"> Experimental Results</p>
                            <p id="dir2p2j"class="mlyj" style="color:#ffffff;"> BBa_K3740030</p>
                            <p id="dir2p2j1"class="mlej" style="color:#ffffff;">Design</p>
                            <p id="dir2p2j2"class="mlej" style="color:#ffffff;">Strategy</p>
                            <p id="dir2p2j3"class="mlej" style="color:#ffffff;">Experimental Results</p>
                            <p id="dir2p2j4" class="mlej" style="color:#ffffff;">Learning</p>
                            <p id="dir2p3j"class="mlyj" style="color:#ffffff;"> BBa_K3740044</p>
                            <p id="dir2p3j1"class="mlej" style="color:#ffffff;">Design</p>
                            <p id="dir2p3j2"class="mlej" style="color:#ffffff;">Strategy</p>
                            <p id="dir2p3j3"class="mlej" style="color:#ffffff;">Experimental Results</p>
                
                            <p id="dir3p" class="mlyj" style="color:#ffffff;">Reference</p>
                        </div>
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            <div class="content"
                style="float:left;width: 1173px;margin-left: 397px;margin-top: 100px;padding-left:100px;background-color: #ffffff;text-align: justify;">

                <div class="yj" id="content1">● Overview：</div>  
                <div class="pb">The goal of project is to use optogenetically engineered <i>Gluconacetobacter
                        hansenii</i> to
                    fight
                    with <i>Pseudomonas aeruginosa</i> infection and produce a bacterial cellulose dressing
                    simultaneously. The
                    genetic engineering consists of three modules, antipseudomonal drug production module, c-di-GMP
                    signaling and BC film production module, safety and drug release module.
                    We have so far made a lot of progress in this project. Hereby, we presented a summary of our
                    engineering
                    data. Although this project is still ongoing and improvements are needed to make in some sections,
                    we
                    believe that our work can contribute to the iGEM community.
                </div>  

                <div class="yj" id="content2">● Engineering Success：</div>
                <div class="ej">I. Antipseudomonal drug production module（<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740050">BBa_K3740050</a>）</div>


                <div class="sj">1. Design</div>

                <div class="pb">We designed an antipseudomonal drug production module to specifically combat <i>P.
                        aeruginosa</i>
                    infection. The receptor domain, the translocase domain of pyocin S2 and the nuclease domain of
                    colicin
                    E3
                    are fused together to get a new chimeric bacteriocin termed SE. The antipseudomonal SE protein can
                    target and inhibit <i>P. aeruginosa</i>, even including those harbouring a S2 immunity protein
                    IMM<sub>S2</sub>. IMM<sub>E3</sub>
                    is
                    an immunity protein derived from <i>Escherichia coli</i>. It can bind to the nuclease domain of SE
                    specifically
                    and inhibit its activity, thus rendering the host cell immune to SE. A similar expression level of
                    the
                    antipseudomonal protein SE and the immunity protein IMM is designed to be expressed in the
                    engineered
                    bacteria, thus preventing the bactericidal effect of SE protein on the bacterial chassis itself.
                </div>


                <div id="dir2p1j2Key" class="sj">2. Strategy</div>
                <div class="pb">Two plasmids S2-PET28A and SE-PET28A were initially constructed and introduced into
                    <i>E.
                        coli</i>
                    BL21. Following the induction of lysis protein by IPTG, bacterial cells were in turn disrupted and
                    the
                    supernatant containing the soluble SE proteins was collected. The molecular weight of SE protein was
                    checked by SDS-PAGE while its specificity to <i>P. aeruginosa</i> was also verified using the drop
                    plate
                    assay;
                    In order to improve the antipseudomonal effect, we engineered the RBS to modulate its strength in
                    controlling SE protein expression. Finally, we identified pR-RBS300-SE-B1006-J23118-RBSII-IMM-rrnB
                    T1(<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740050">BBa_K3740050</a>) as our
                    optimal genetic circuit.
                </div>


                <image src="https://2021.igem.org/wiki/images/8/8b/T--SZPT-CHINA--Engineering-pic-1.png" class="pic"
                    style="margin-left: 137px;">

                </image>
                <div class="tz">Figure 1. The gene circuit of pR-RBS300-SE-B1006-J23118-RBSII-IMM- rrnB T1
                    (<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740050">BBa_K3740050</a>)
                </div>

                <div id="dir2p1j3Key" class="sj" >3. Experimental results:</div>
                <div class="ssj">3.1 Sequencing</div>

                <div class="pb">Plasmids from <i>E. coli</i> cells were extracted and sequenced. Analysis based on
                    sequencing
                    data indicated that the SE-encoded sequence and pR-RBS300-SE-B1006-J23118-RBSII-IMM-rrnB T1
                    (<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740050">BBa_K3740050</a>) have been
                    successfully integrated into the plasmid vectors.</div>

                <div class="ssj">3.2 Characterization of fusion protein SE</div>

                <div class="wj">3.2.1 SDS-PAGE</div>

                <div class="pb">Method: IPTG was added to a final concentration of 0.1 mmol/mL to induce SE protein
                    expression in <i>E. coli</i> BL21 and subsequently incubated at 25℃ for 12 hours. Supernatant
                    containing SE
                    or
                    S2 proteins was obtained by sonication and centrifugation respectively. The crude protein extract
                    was
                    loaded into SDS-PAGE gel and stained by Coomassie Blue to verify the presence of target proteins
                    (For
                    more detailed steps, please click <a
                        href="https://2021.igem.org/Team:SZPT-CHINA/Experiments">Experiments</a>).
                    <br><br>
                    After induction by IPTG, S2 and SE protein expression in S2-PET28A-BL21 (lane 2) and SE-PET28A-BL21
                    (lane 3) has been identified. By contrast, target proteins were not expressed in the strain with
                    S2-PET28A-BL21 (lane 1) and SE -PET28A-BL21 (lane 4) in the absence of IPTG, <strong> indicating
                        that
                        expression
                        of S2 and SE proteins can be successfully induced in <i>E. coli</i> transformed with S2-PET28A
                        and
                        SE-PET28A,
                        respectively.</strong>
                </div>

                <image src="https://2021.igem.org/wiki/images/4/4b/T--SZPT-CHINA--Engineering-pic-2.png" class="pic"
                    style="margin-left: 312px;width: 500px;">
                </image>

                <div class="tz">Figure 2. SDS-PAGE analysis of protein expression in engineered <i>E. coli</i> BL21.
                    Lane 1,
                    S2-PET28A-BL21 without IPTG induction; Lane 2, S2-PET28A-BL21 with induction by 0.1mmol/mL IPTG;
                    Lane 3,
                    SE-PET28A-BL21 with induction by 0.1mmol/mL IPTG; Lane 4, SE-PET28A-BL21 without IPTG induction.
                </div>

                <div class="wj">3.2.2 SE protein targeting verification</div>

                <div class="pb">Method: Supernatant containing SE or S2 protein was respectively mixed with the culture
                    of
                    <i>Pseudomonas aeruginosa</i> PAO1, <i>P. aeruginosa</i> PAO1Δ1150-1151(PAO1 Δ1150-1151, PAO1
                    knocked out
                    of
                    S2+IMM<sub>S2</sub>)
                    and <i>E. coli</i> MG1655. PBS was used as a negative control. Inhibitory effect of supernatant on
                    the <i>P.
                        aeruginosa</i> growth was determined by measuring OD<sub>600</sub> using SYNERGY H1 micro-plate
                    reader. (For more
                    detailed steps, please click <a
                        href="https://2021.igem.org/Team:SZPT-CHINA/Experiments">Experiments</a>)
                    <br><br>
                    We found that the OD<sub>600</sub> values of both <i>P. aeruginosa</i> strains cultured with SE
                    protein, were
                    much
                    lower
                    than that of the control group PBS. This proves that SE protein has antipseudomonal properties. In
                    contrast, pyocin S2 could only act on the immune-deficiency strain PAO1∆1150-1151. This proves that
                    SE
                    protein has a broader antipseudomonal spectrum than S2. Meanwhile, the OD<sub>600</sub> value of
                    <i>E. coli</i>
                    MG1655
                    cultured with SE protein was a little higher than that of the control group PBS. This indicates that
                    SE
                    protein does not work on <i>E. coli</i>. <strong> This result indicated that the fusion protein SE
                        can
                        specifically
                        kill
                        <i> P. aeruginosa</i></strong>.
                </div>


                <image src="https://2021.igem.org/wiki/images/2/25/T--SZPT-CHINA--Engineering-pic-3.png" class="pic"
                    style="margin-left: 300px;">
                </image>

                <div class="tz">Figure 3. Optical density of bacterial culture of PAO1, PAO1 Δ1150-1151 and <i>E.
                        coli</i>
                    MG1655
                    treated by the supernatant of S2-PET28A-BL21 or SE-PET28A-BL21 for 790 minutes. PBS was used as the
                    negative control.</div>

                <div class="ssj">3.3 Batch screening and verification of SE protein antibacterial performance of
                    composite
                    parts</div>
                <div class="pb">Method: PAO1 growth inhibition verification. <i>G. hansenii</i> ATCC 53582 culture
                    supernatant
                    containing SE proteins that were expressed under control of different RBS were obtained by
                    sonication
                    and centrifugation and further purified by infiltration with micro-pored membrane. Then, supernatant
                    in
                    different groups was individually mixed with PAO1 culture, and incubated at 30℃ for 12 hours.
                    SYNERGY H1
                    micro-plate reader was used to measure the OD<sub>600</sub> to determine the effect on PAO1 growth.
                    Inhibition zone experiment. 3<i>μL</i> of the supernatant containing SE protein was dropped on FAB
                    plate
                    with
                    PAO1（For more detailed steps, please click <a
                        href="https://2021.igem.org/Team:SZPT-CHINA/Experiments">Experiments</a>).
                    <br>
                    <br>
                    As shown in Figure 4 (a), we found that the OD<sub>600</sub> values of PAO1 strains cultured with
                    supernatant
                    of
                    the 3<sup>rd</sup>, 4<sup>th</sup>, 7<sup>th</sup>, and 8<sup>th</sup> colonies bacterial lysate,
                    were much lower than that of PBS in the control
                    group. This proves that culture supernatant of the 3<sup>rd</sup>, 4<sup>th</sup>, 7<sup>th</sup>,
                    and 8<sup>th</sup> colonies had a remarkable
                    inhibitory effect on the growth of PAO1. Consistent with this result, supernatants from all the
                    <i>G.
                        hansenii</i> isolates have formed inhibition zone on the plate spread with PAO1, yet with
                    different
                    sizes.
                    The 3<sup>rd</sup> and 4<sup>th</sup> isolate displayed the most significant antipseudomonal effect,
                    while the control,
                    the
                    9<sup>th</sup> colony had no effect. Taken together, <strong> these results show that expression of
                        SE protein was
                        successfully induced in <i>G. hansenii</i> ATCC 53582. Besides, by adjusting the RBS upstream
                        the
                        SE-encoded
                        sequence, we screened and identified that the 4th strain,
                        pR-RBS300-SE-B1006-J23118-RBSII-IMM-rrnB
                        T1-pSEVA331-<i>G. hansenii</i> ATCC 53582-4# exhibited the optimal antipseudomonal
                        effect.</strong>
                </div>

                <image src="https://2021.igem.org/wiki/images/4/4c/T--SZPT-CHINA--Engineering-pic-4.png" class="pb"
                    style="width: 1244px;">
                </image>
                <div class="tz">Figure 4. (a) Optical density of bacterial culture of PAO1 treated by the supernatant of
                    engineered strains for 790 minutes. (b) Inhibition zone test. (c) Strains are used for Figure(a) and
                    Figure(b).</div>

                <div class="ssj">3.4 Video shooting</div>


                <video src="https://2021.igem.org/wiki/images/2/20/T--SZPT-CHINA--Engineering-video-1.mp4" controls
                    style="margin-top: 50px;margin-left: 275px;"> </video>

                <div class="tz">Video 1. Video shooting of the zone of inhibition of 4th bacteria:
                    pR-RBS300-SE-J23118-RBSII- IMM-rrnB T1-pSEVA331-<i>G. hansenii</i> ATCC 53582-4#.</div>

                <div class="ej">II. C-di-GMP signaling and BC film production module (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740030">BBa_K3740030</a>)</div>

                <div id="dir2p2j1Key" class="sj">1. Design</div>
                <div class="pb">This c-di-GMP signaling and BC film production module has two submodules. One is the
                    diguanylate cyclase sub-module, which regulates the synthesis of c-di-GMP. The bacterial phytochrome
                    BphS is utilized to synthesize c-di-GMP in a light-dependent manner, thereby controlling BC film
                    production in <i>G. hansenii</i> ATCC 53582. The other is c-di-GMP phosphodiesterase sub-module,
                    which
                    regulates the hydrolysis of c-di-GMP. By screening different parts, the level of c-di-GMP in
                    bacteria
                    can remain in a low level or even close to zero under the dark condition.</div>
                <div id="dir2p2j2Key" class="sj">2. Strategy</div>
                <div class="pb">A series of plasmids derived from J23100-B0034 were constructed and transferred into
                    <i>G.
                        hansenii</i> ATCC 53582, in which the BC film production was quantified. Finally, fcsR (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740022">BBa_K3740022</a>)
                    was
                    selected as the c-di-GMP phosphodiesterase encoding gene. Different promoters were then used to
                    direct
                    the expression of FcsR. Based on the screening results, <a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740030">BBa_K3740030</a>,
                    <a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740031">BBa_K3740031</a> and
                    <a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740043">BBa_K3740043</a>
                    were
                    constructed and introduced into <i>G. hansenii</i> ATCC 53582 through electroporation. Finally, BC
                    film
                    production was assessed in these strains.
                </div>

                <image src="https://2021.igem.org/wiki/images/0/01/T--SZPT-CHINA--Engineering-pic-5.png" class="pic"
                    style="margin-left: 159px;">
                </image>
                <div class="tz">Figure 5. The gene circuit of J23100-B0034-bphS-pET RBS-bphO-rrnB T1-J23109-B0034-fcsR-
                    rrnB
                    T1 (<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740030">BBa_K3740030</a>).</div>

                <div id="dir2p2j3Key" class="sj">3. Experimental results</div>
                <div class="ssj">3.1 Agarose gel electrophoresis</div>
                <div class="pb">As shown in Figure 6 (a), c-di-GMP phosphodiesterase-encoded genes (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740065">BBa_K3740065</a>),
                    (<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740062">BBa_K3740062</a>)
                    and (<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740066">BBa_K3740066</a>) were
                    identified successfully by PCR amplification and c-di-GMP diguanylate
                    cyclase-encoded genes (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740047">BBa_K3740047</a>) was
                    identified by PCR amplication; As shown in Figure 6(b),
                    composite
                    parts including (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740030">BBa_K3740030</a>), (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740031">BBa_K3740031</a>)
                    and (<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740043">BBa_K3740043</a>) were
                    identified successfully by PCR.
                </div>


                <image src="https://2021.igem.org/wiki/images/0/01/T--SZPT-CHINA--Engineering-pic-6.png" class="pic"
                    style="width: 1230px;">
                </image>
                <div class="tz">Figure 6. (a), (b)The agarose gel electrophoresis image of the constructed plasmid after
                    PCR
                    amplification. (c)Plasmids are used for Figure(a) and Figure(b).</div>

                <div class="ssj">3.2 Film production verification experiment</div>

                <div class="wj">3.2.1 Film production verification experiment of bphS and fcsR</div>

                <div class="pb">Method: The constructed plasmids were introduced into <i>G. hansenii</i> ATCC 53582 and
                    cultured at
                    30°C. Then a single colony was picked to launch its liquid culture. Then the culture was distributed
                    in
                    two copies of 12-well plates, with one under NIR light illumination and the other under dark
                    condition
                    for 4 days. (For more detailed steps, please click <a
                        href="https://2021.igem.org/Team:SZPT-CHINA/Experiments">Experiments</a>)
                    <br><br>
                    As shown in Figure 7 (a), BC production in J23100-fcsR-rrnB T1-pSEVA331- <i>G. hansenii</i> ATCC
                    53582 and
                    the
                    control group pSEVA331- <i>G. hansenii</i> ATCC 53582 were different, indicating that FcsR was
                    capable of
                    hydrolyzing c-di-GMP in <i>G. hansenii</i>. While, J23100-bphS-pET RBS-bphO-rrnB T1-pSEVA331-<i>G.
                        hansenii</i>
                    ATCC
                    53582, produced a higher level of BC film under near-infrared light than that under dark condition,
                    indicating that BphS in <i>G. hansenii</i> ATCC 53582 can synthesize c-di-GMP. <strong> To
                        summarize, BphS
                        and FcsR
                        were
                        opted as the c-di-GMP synthetase and hydrolase in our system, respectively.</strong>
                </div>


                <image src="https://2021.igem.org/wiki/images/e/e4/T--SZPT-CHINA--Engineering-pic-7.png" class="pic"
                    style="margin-left: 288px;">
                </image>
                <div class="tz">Figure 7. (a)BC yield by J23100-B0034-fcsR-rrn B T1-pSEVA331-<i>G. hansenii</i> ATCC
                    53582,
                    J23100-B0034-yhjH-rrnB T1-pSEVA331-<i>G. hansenii</i> ATCC 53582, J23100-B0034-rocR-rrnB
                    T1-pSEVA331-<i>G.
                        hansenii</i>
                    ATCC 53582 and the vehicle control pSEVA331-<i>G. hansenii</i> ATCC 53582; (b) BC yield by
                    J23100-bphS-pET
                    RBS-bphO-rrnB T1-pSEVA331-<i>G. hansenii</i> ATCC 53582 under NIR light illumination and dark
                    condition.
                </div>
                <div class="wj">3.2.2 Film production verification experiment of bphS-fcsR</div>
                <div class="pb">A significant difference in BC film production under NIR light and dark conditions were
                    observed for those strains, including J23100-B0034-bphS-pET RBS-bphO-rrnB T1-J23109-B0034-fcsR-rrnB
                    T1-pSEVA331-<i>G. hansenii</i> ATCC 53582, J23100-B0034-bphS-pET RBS-bphO-rrnB
                    T1-J23110-B0034-fcsR-rrnB
                    T1-pSEVA331-<i>G. hansenii</i> ATCC 53582, however J23100-B0034-bphS-pET RBS-bphO-rrnB
                    T1-J23119-B0034-fcsR-rrnB
                    T1-pSEVA331-<i>G. hansenii</i> ATCC 53582 had no difference in BC film production under NIR light
                    and dark
                    conditions, <strong> these results showed that J23100-B0034-bphS-pET RBS-bphO-rrnB
                        T1-J23109-B0034-fcsR-rrnB
                        T1-pSEVA331-<i>G. hansenii</i> ATCC 53582 and J23100-B0034-bphS-pET RBS-bphO-rrnB
                        T1-J23110-B0034-fcsR-rrnB
                        T1-pSEVA331-<i>G. hansenii</i> ATCC 53582 can be used as our gene circuit.</strong></div>

                <image src="https://2021.igem.org/wiki/images/5/57/T--SZPT-CHINA--Engineering-pic-8.png" class="pic"
                    style="width: 1230px;">
                </image>

                <div class="tz">Figure 8. (a) BC film production by different strains, (b) Strains are used for
                    Figure(a).
                </div>
                <div class="ssj">3.3 Video shooting</div>


                <video src="https://2021.igem.org/wiki/images/5/59/T--SZPT-CHINA--Engineering-video-2.mp4" controls
                    style="margin-top: 50px;margin-left: 94px;width: 1000px;"> </video>


                <div class="tz">Video 2. Video shooting of J23100-B0034-bphS-pET RBS-bphO-rrnB T1-J23109-B0034-fcsR-rrnB
                    T1-pSEVA331-<i>G. hansenii</i> ATCC 53582 bacterial BC production.</div>



                <div id="dir2p2j4Key" class="sj">4. Learning:</div>
                <div class="pb">In our film production assay, the film production by engineered bacteria under dark
                    condition was expected to remain at a very low level. Surprisingly, a substantial amount of BC film
                    was
                    still found without NIR light induction, even though the level was lower than that in the
                    NIR-induced
                    group. In the future, we will solve this problem and refine the genetic circuit.</div>


                <div class="ej">III. Safety and drug release module (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740044">BBa_K3740044</a>)</div>


                <div id="dir2p3j1Key" class="sj">1. Design</div>
                <div class="pb">This module is a dual design of both safety control and drug release. We use pDawn, a
                    blue-light-responsive promoter to direct the expression of the lytic proteins, which would cause the
                    lysis
                    and death of the engineered bacteria. Then, SE protein expressed within the engineered bacteria will
                    be
                    released.
                    We have constructed a set of plasmids which include pDawn to induce the expression of an
                    anti-holin-free
                    Lambda lysis cassette (S105), φX174 lysis gene (X174 E), and LKD16 lysis cassette (LKD16). They were
                    chosen
                    to lyse our chassis bacteria. After screening, X174 E (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2656015">BBa_K2656015</a>) was
                    selected as the final part
                    in
                    our
                    safety and drug release module.
                </div>
                <div id="dir2p3j2Key"class="sj">2. Strategy</div>
                <div class="pb">RFP was firstly used to verify the responsiveness of the pDawn promoter to blue light.
                    Then,
                    random primer guided mutagenesis method to modulate the strength of the RBS (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_B0034">BBa_B0034</a>) located
                    upstream
                    of
                    X174 E. Finally, the pDawn-RBSNNN-X174 E-rrnB T1 (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740044">BBa_K3740044</a>) plasmid
                    was constructed and
                    introduced
                    into
                    <i>E. coli</i>. <i>E. coli</i> isolates that grow normally in the dark and cannot grow under blue
                    light
                    were
                    screened
                    out.
                    Finally, the plasmid was extracted, and further introduced into <i>G. hansenii</i> ATCC 53582, in
                    which the
                    responsiveness of pDawn to blue light was also verified.
                </div>

                <image src="https://2021.igem.org/wiki/images/f/fc/T--SZPT-CHINA--Engineering-pic-9.png" class="pic"
                    style="margin-left: 306px;">
                </image>

                <div class="tz">Figure 9. The gene circuit of pDawn-RBSNNN-X174 E-rrnB T1 (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740044">BBa_K3740044</a>).
                </div>

                <div id="dir2p3j3Key" class="sj">3.Experimental results</div>

                <div class="ssj">3.1 The pDawn promoter responds to blue light verification in <i>G. hansenii</i> ATCC
                    53582
                </div>
                <div class="pb">Red fluorescence could be observed in the pDawn-B0034-RFP-rrnB T1-pSEVA331-<i>G.
                        hansenii</i>
                    ATCC
                    53582 under 470-nm blue light, but there was no red fluorescence under dark condition,<strong>
                        suggesting
                        that
                        the pDawn promoter could respond to blue light and induce gene expression in <i>G. hansenii</i>
                        ATCC
                        53582.</strong>
                </div>

                <image src="https://2021.igem.org/wiki/images/1/1f/T--SZPT-CHINA--Engineering-pic-10.png" class="pic"
                    style="margin-left: 197px;">
                </image>
                <div class="tz">Figure 10. Red fluorescence photo of the pDawn-B0034-RFP-rrnB T1-pSEVA331-<i>G.
                        hansenii</i>
                    ATCC
                    53582 cultured under 470-nm blue light (a) or dark condition (b) for 24 hours. </div>
                <div class="ssj">3.2 Batch screening of pDawn-RBSNNN- X174 E-rrnB T1-pSEVA331 in response to blue light
                    lysis
                    in <i>E. coli</i></div>
                <div class="pb">
                    Method: We use the random primer method to modulate the strength of the RBS (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_B0034">BBa_B0034</a>) located
                    upstream
                    of X174 E. After introducing into <i>E. coli </i>DH5α, a drop plate assay was performed to screen
                    the
                    bacterial
                    isolate that can grow normally in the dark but cannot under the blue light irradiation.
                    <br><br>
                    As shown in Figure 11, the 4th isolate that grew normally in the dark but did not under blue light,
                    <strong> indicating that we successfully expressed the cleavage protein X174 E in <i>E. coli.</i>
                    </strong>
                </div>
                <image src="https://2021.igem.org/wiki/images/9/9e/T--SZPT-CHINA--Engineering-pic-11.png" class="pic"
                    style="margin-left: 231px;">
                </image>
                <div class="tz">Figure 11：The growth status of pDawn-RBSNNN-X174 E-rrnB T1-pSEVA331-DH5α under blue
                    light
                    (a)
                    and dark condition (b).</div>


                <div class="ssj">3.3 pDawn-RBSNNN-X174 E-rrnB T1-pSEVA331-7# in response to blue photolysis in <i>G.
                        hansenii</i>
                    ATCC 53582</div>


                <div class="pb">Method: We launched the liquid culture of pDawn-RBSNNN-X174 E-rrnB T1-pSEVA331-DH5α,
                    extracted the plasmid and introduced into <i>G. hansenii</i> ATCC 53582. After 2 days of incubation,
                    we
                    selected 20 monoclonal to spot on two parallel new plates, which were incubated for another 2 days,
                    with
                    one under blue light and the other in the dark. The strains with obvious growth difference under
                    different illumination conditions were preserved. The drop plate assay using this strain was
                    repeated to
                    verify the lysis effect of X174 E on <i>G. hansenii</i> ATCC 53582.
                    <br><br>
                    As shown in Figure 12 (a), <i>G. hansenii</i> ATCC 53582 strains under the dark condition exhibited
                    better
                    growth than those under blue light irradiation; (b) pDawn-RBSNNN-X174 E-rrnB T1-pSEVA331-<i>G.
                        hansenii</i>
                    ATCC
                    53582-7# showed a stable lysis effect under blue light illumination but not in the dark, indicating
                    that
                    we successfully expressed the cleavage protein X174 E in <i>G. hansenii</i> ATCC 53582.
                </div>



                <image src="https://2021.igem.org/wiki/images/7/7d/T--SZPT-CHINA--Engineering-pic-12.png" class="pic">
                </image>
                <div class="tz">Figure 12. (a) The growth status of pDawn-RBSNNN-X174 E-rrnB T1-pSEVA331-<i>G.
                        hansenii</i> ATCC
                    53582-4# under blue light (1) and dark conditions (2), (b)The growth status of pDawn-RBSNNN-X174
                    E-rrnB
                    T1-pSEVA331-<i>G. hansenii</i> ATCC 53582-7# under blue light (1) and dark conditions (2).</div>
                <div class="pb">In our safety and drug release module, we verified the lysis effect of (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740024">BBa_K3740024</a>) and
                    (<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740032">BBa_K3740032</a>), however
                    their effect was inferior to that of (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K2656015">BBa_ K2656015</a>). If you
                    are interested in
                    our
                    other two parts, please Click: (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740033">BBa_K3740033</a>) and (<a
                        href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K3740051">BBa_K3740051</a>).</div>

                <div id="dir3pKey" class="ej">Reference</div>
                <div class="pb">
                    [1] Gupta S, Bram E E, Weiss R. Genetically programmable pathogen sense and destroy. [J]. Acs
                    Synthetic
                    Biology, 2013, 2(12): 715-723.<br>
                    [2] Jin F, Gao YM, Huang YJ, et al. Current therapies for <i>Pseudomonas aeruginosa</i> infection
                    [J].
                    Journal
                    of Integration Technology, 2021, 10(4): 50-66.<br>
                    [3] Michel-Briand Y, Baysse C. The pyocins of <i>Pseudomonas aeruginosa.</i> [J]. Biochimie, 2002,
                    84(5-6): 499-510.<br>
                    [4] Denayer S, Matthijs S, Cornelis P. Pyocin S2 (Sa) Kills <i>Pseudomonas aeruginosa</i> Strains
                    via the
                    FpvA
                    Type I Ferripyoverdine Receptor [J]. Journal of Bacteriology, 2007, 189(21): 7663.<br>
                    [5] Ryu M H, Gomelsky M Near-infrared Light Responsive Synthetic c-di-GMP Module for Optogenetic
                    Applications [J]. Acs Synthetic Biology, 2014, 3(11): 802<br>
                    [6] Elaheh Sajadi,Seyed Safa-Ali Fatemi,Valiollah Babaeipour,Ali Asghar Deldar,Bagher
                    Yakhchali,Mohammad
                    Saberi Anvar. Increased cellulose production by heterologous expression of bcsA and B genes from
                    Gluconacetobacter xylinus in <i>E. coli</i> Nissle 1917 [J]. Bioprocess and Biosystems
                    Engineering, 2019, 42(12):
                    2023-2034.<br>
                    [7] Jin X, Riedel-Kruse I H. Biofilm Lithography enables high-resolution cell patterning via
                    optogenetic
                    adhesin expression [J]. Proceedings of the National Academy of Sciences of the United States of
                    America,
                    2018: 3698-3703.<br>
                    [8] Ceyssens P J, Lavigne R, Mattheus W, et al. Genomic Analysis of <i>Pseudomonas aeruginosa</i>
                    Phages
                    LKD16
                    and LKA1: Establishment of the KMV Subgroup within the T7 Supergroup [J]. Journal of Bacteriology,
                    2006.<br>
                    [9] Yibo S, Jianhe S, Shi Y, et al. Current advance in the topological structure and function of
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                    encoded by bacteriophage lambda [J]. Acta Microbiologica Sinica, 2012, 52(2): 141-145.<br>
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                    <i>Escherichia
                        coli</i> [J]. Archives of Microbiology, 1992, 157(4): 381-388.<br>
                    [11] Ohlendorf R, Vidavski R R, Eldar A, et al. From dusk till dawn: one-plasmid systems for
                    light-regulated gene expression [J]. Journal of Molecular Biology, 2012, 416(4): 534-542.

                </div>


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